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Structure, Activity and Function of the Protein Arginine Methyltransferase 6

Members of the protein arginine methyltransferase (PRMT) family methylate the arginine residue(s) of several proteins and regulate a broad spectrum of cellular functions. Protein arginine methyltransferase 6 (PRMT6) is a type I PRMT that asymmetrically dimethylates the arginine residues of numerous...

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Autores principales: Gupta, Somlee, Kadumuri, Rajashekar Varma, Singh, Anjali Kumari, Chavali, Sreenivas, Dhayalan, Arunkumar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8470942/
https://www.ncbi.nlm.nih.gov/pubmed/34575100
http://dx.doi.org/10.3390/life11090951
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author Gupta, Somlee
Kadumuri, Rajashekar Varma
Singh, Anjali Kumari
Chavali, Sreenivas
Dhayalan, Arunkumar
author_facet Gupta, Somlee
Kadumuri, Rajashekar Varma
Singh, Anjali Kumari
Chavali, Sreenivas
Dhayalan, Arunkumar
author_sort Gupta, Somlee
collection PubMed
description Members of the protein arginine methyltransferase (PRMT) family methylate the arginine residue(s) of several proteins and regulate a broad spectrum of cellular functions. Protein arginine methyltransferase 6 (PRMT6) is a type I PRMT that asymmetrically dimethylates the arginine residues of numerous substrate proteins. PRMT6 introduces asymmetric dimethylation modification in the histone 3 at arginine 2 (H3R2me2a) and facilitates epigenetic regulation of global gene expression. In addition to histones, PRMT6 methylates a wide range of cellular proteins and regulates their functions. Here, we discuss (i) the biochemical aspects of enzyme kinetics, (ii) the structural features of PRMT6 and (iii) the diverse functional outcomes of PRMT6 mediated arginine methylation. Finally, we highlight how dysregulation of PRMT6 is implicated in various types of cancers and response to viral infections.
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spelling pubmed-84709422021-09-27 Structure, Activity and Function of the Protein Arginine Methyltransferase 6 Gupta, Somlee Kadumuri, Rajashekar Varma Singh, Anjali Kumari Chavali, Sreenivas Dhayalan, Arunkumar Life (Basel) Review Members of the protein arginine methyltransferase (PRMT) family methylate the arginine residue(s) of several proteins and regulate a broad spectrum of cellular functions. Protein arginine methyltransferase 6 (PRMT6) is a type I PRMT that asymmetrically dimethylates the arginine residues of numerous substrate proteins. PRMT6 introduces asymmetric dimethylation modification in the histone 3 at arginine 2 (H3R2me2a) and facilitates epigenetic regulation of global gene expression. In addition to histones, PRMT6 methylates a wide range of cellular proteins and regulates their functions. Here, we discuss (i) the biochemical aspects of enzyme kinetics, (ii) the structural features of PRMT6 and (iii) the diverse functional outcomes of PRMT6 mediated arginine methylation. Finally, we highlight how dysregulation of PRMT6 is implicated in various types of cancers and response to viral infections. MDPI 2021-09-11 /pmc/articles/PMC8470942/ /pubmed/34575100 http://dx.doi.org/10.3390/life11090951 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Gupta, Somlee
Kadumuri, Rajashekar Varma
Singh, Anjali Kumari
Chavali, Sreenivas
Dhayalan, Arunkumar
Structure, Activity and Function of the Protein Arginine Methyltransferase 6
title Structure, Activity and Function of the Protein Arginine Methyltransferase 6
title_full Structure, Activity and Function of the Protein Arginine Methyltransferase 6
title_fullStr Structure, Activity and Function of the Protein Arginine Methyltransferase 6
title_full_unstemmed Structure, Activity and Function of the Protein Arginine Methyltransferase 6
title_short Structure, Activity and Function of the Protein Arginine Methyltransferase 6
title_sort structure, activity and function of the protein arginine methyltransferase 6
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8470942/
https://www.ncbi.nlm.nih.gov/pubmed/34575100
http://dx.doi.org/10.3390/life11090951
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